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Database: UniProt/TrEMBL
Entry: A0A0D6AFK4_9CHRO
LinkDB: A0A0D6AFK4_9CHRO
Original site: A0A0D6AFK4_9CHRO 
ID   A0A0D6AFK4_9CHRO        Unreviewed;      1014 AA.
AC   A0A0D6AFK4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=GM3708_1979 {ECO:0000313|EMBL:BAQ61573.1};
OS   Geminocystis sp. NIES-3708.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Chroococcaceae; Geminocystis.
OX   NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ61573.1, ECO:0000313|Proteomes:UP000060542};
RN   [1] {ECO:0000313|EMBL:BAQ61573.1, ECO:0000313|Proteomes:UP000060542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ61573.1,
RC   ECO:0000313|Proteomes:UP000060542};
RA   Hirose Y.;
RT   "Geminocystis sp. NIES-3708 complete genome sequence.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; AP014815; BAQ61573.1; -; Genomic_DNA.
DR   EnsemblBacteria; BAQ61573; BAQ61573; GM3708_1979.
DR   KEGG; gee:GM3708_1979; -.
DR   PATRIC; fig|1615909.3.peg.2012; -.
DR   KO; K01595; -.
DR   Proteomes; UP000060542; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 2.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000060542};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:BAQ61573.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060542}.
FT   ACT_SITE    191    191       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    661    661       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1014 AA;  116869 MW;  A2D9252814696228 CRC64;
     MTSAMTNYTE ELSIYSSSEL LLRHRLKLVE NLWESVLTNE CGQELVDLLD KLKSACSPEG
     QTNETQNISV SKWIEQLELD DAIKAVRAFA LYFQLINIVE QHYEQRTQKL IRRTTTEDQV
     NAIQKPESHN HQPTTLDTKE EAQSYFNPKS NPASGGTFHW LFPYLQKLNM PPPKIQQLLD
     QLDINLVFTA HPTEIVRHTI RKKQRRISHF LEKLDAAEES FRAMGLTNSW EAENYRECLT
     EEVRLWWRTD ELHQFKPTVL DEVDYALHYF QEVLFQTLPE LSIRLKQALH NTFPKLKSPT
     HKFCYFGSWV GGDRDGNPFV TPEVTWSTAC YQRNLVIDKY LESMGQLNDI LSLSLHWCNV
     MPELLDSLER DRIGMPELYD KLYVRYRQEP YRLKLAYIEQ RLKNTQVRNE ALSDPETRKS
     IKLANKDDSL YPSKLDLLED LNLIKYNLEN TGLKCKELDH LISQVEIFGF HLTPLDFRQD
     SSRHSDALSE IAEYLGVLDK PYEELSETEK TAWLVQELKT RRPLIPSEIN FSDATGETIE
     TFKILRALQT EFGLDICHTY IISMTNYVSD VLEVLLLAKE AGLYDPILGI TSIRIVPLFE
     TVEDLKRAPM VMTELFELPL YRACLAGGYE NVAKLPSNLV LPELNPKNLQ EIMLGYSDSN
     KDSGFLSSNW EIHKAQKTLA RIGDKYGFNI KIFHGRGGSV GRGGGPAYAA ILAQPTSTID
     GRIKITEQGE VLASKYSLPE LALYNLETIS TAVIQASLLG SGFDDIEPWN QIMEEIAAYS
     RKAYRQLIYE QPDFIDFFLS VTPIEEISKL QISSRPARRS SGKKDISSLR AIPWVFSWTQ
     SRFLLPAWYG VGTALQEFLN QEPEENLKLL RYFYLKWPFF KMVISKAEMT LSKVDLQMAS
     HYVDELAKDE DKERFQKVFN QIAKEYYLSR DIVLQINEQE RLLDNDPELQ RSVQLRNGTI
     VPLGFLQVSL LKRLRQYASQ DKAGLIHFRY SKEELLRGAL LTINGIAAGM RNTG
//
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